Structure of PDB 1d1v Chain A

Receptor sequence

>1d1vA (length=416) Species: 9913 (Bos taurus)

GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPS
PGPPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYH
LRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNH
IKYATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGD
PANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVP
LEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGT
RNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAK
VTIVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEM
VNYILSPAFRYQPDPW

3D structure

• PDB: 1d1v Implications for isoform-selective inhibitor design derived from the binding mode of bulky isothioureas to the heme domain of endothelial nitric-oxide synthase.
• Chain: A
• Resolution: 1.93 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C186 R189 W358 E363
• Catalytic site (residue number reindexed from 1): C120 R123 W292 E297
• Enzyme Commision number: 1.14.13.39: nitric-oxide synthase (NADPH).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	C96 C101	C30 C35
BS02	HEM	A	W180 R185 C186 F355 S356 W358 E363 W449 Y477	W114 R119 C120 F289 S290 W292 E297 W383 Y411
BS03	H4B	A	S104 R367 A448 W449	S38 R301 A382 W383
BS04	PTU	A	P336 V338 F355 W358 E363	P270 V272 F289 W292 E297

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:1d1v, PDBe:1d1v, PDBj:1d1v
• PDBsum: 1d1v
• PubMed: 11331290
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)